CDAC1_HUMAN
ID CDAC1_HUMAN Reviewed; 514 AA.
AC Q9BWV3; Q49A08; Q4G119; Q5TAW9; Q7Z764; Q9NT36;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cytidine and dCMP deaminase domain-containing protein 1;
DE EC=3.5.4.5 {ECO:0000269|PubMed:26945630};
DE AltName: Full=Cytidine deaminase {ECO:0000305};
DE AltName: Full=Testis development protein NYD-SP15;
GN Name=CDADC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=16955368; DOI=10.1007/s10528-006-9038-x;
RA Liu Q., Liu J., Cao Q., Sha J., Zhou Z., Wang H., Li J.;
RT "NYD-SP15: a novel gene potentially involved in regulating testicular
RT development and spermatogenesis.";
RL Biochem. Genet. 44:409-423(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Bone marrow, Brain, Pancreas, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 400-514.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MOTIF.
RX PubMed=26945630; DOI=10.1016/j.gene.2016.02.048;
RA Xu Y., Li L., Li J., Liu Q.;
RT "Structural and biological function of NYD-SP15 as a new member of cytidine
RT deaminases.";
RL Gene 583:36-47(2016).
CC -!- FUNCTION: Catalyzes the deamination of cytidine and deoxycytidine into
CC uridine and deoxyuridine, respectively (PubMed:26945630). May play an
CC important role in testicular development and spermatogenesis
CC (PubMed:16955368). {ECO:0000269|PubMed:16955368,
CC ECO:0000269|PubMed:26945630}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+);
CC Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC Evidence={ECO:0000269|PubMed:26945630};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine + H(+) + H2O = NH4(+) + uridine;
CC Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938; EC=3.5.4.5;
CC Evidence={ECO:0000269|PubMed:26945630};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9GZX7};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:26945630}. Nucleus
CC {ECO:0000305|PubMed:26945630}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BWV3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BWV3-2; Sequence=VSP_027812, VSP_027813;
CC Name=3;
CC IsoId=Q9BWV3-3; Sequence=VSP_027814, VSP_027815;
CC Name=4;
CC IsoId=Q9BWV3-4; Sequence=VSP_027811;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in the
CC testis. {ECO:0000269|PubMed:16955368}.
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. {ECO:0000305}.
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DR EMBL; AY027525; AAK16745.1; -; mRNA.
DR EMBL; AL138875; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08817.1; -; Genomic_DNA.
DR EMBL; BC009562; AAH09562.1; -; mRNA.
DR EMBL; BC032889; AAH32889.1; -; mRNA.
DR EMBL; BC048092; AAH48092.1; -; mRNA.
DR EMBL; BC125202; AAI25203.1; -; mRNA.
DR EMBL; AL137554; CAB70808.1; -; mRNA.
DR CCDS; CCDS9415.1; -. [Q9BWV3-1]
DR PIR; T46393; T46393.
DR RefSeq; NP_001180407.1; NM_001193478.1.
DR RefSeq; NP_112173.1; NM_030911.3. [Q9BWV3-1]
DR AlphaFoldDB; Q9BWV3; -.
DR SMR; Q9BWV3; -.
DR BioGRID; 123540; 12.
DR IntAct; Q9BWV3; 2.
DR STRING; 9606.ENSP00000251108; -.
DR iPTMnet; Q9BWV3; -.
DR PhosphoSitePlus; Q9BWV3; -.
DR BioMuta; CDADC1; -.
DR DMDM; 74724888; -.
DR EPD; Q9BWV3; -.
DR MassIVE; Q9BWV3; -.
DR PaxDb; Q9BWV3; -.
DR PeptideAtlas; Q9BWV3; -.
DR PRIDE; Q9BWV3; -.
DR ProteomicsDB; 79325; -. [Q9BWV3-1]
DR ProteomicsDB; 79326; -. [Q9BWV3-2]
DR ProteomicsDB; 79327; -. [Q9BWV3-3]
DR ProteomicsDB; 79328; -. [Q9BWV3-4]
DR Antibodypedia; 23898; 180 antibodies from 21 providers.
DR DNASU; 81602; -.
DR Ensembl; ENST00000251108.10; ENSP00000251108.6; ENSG00000102543.14. [Q9BWV3-1]
DR GeneID; 81602; -.
DR KEGG; hsa:81602; -.
DR MANE-Select; ENST00000251108.10; ENSP00000251108.6; NM_030911.4; NP_112173.1.
DR UCSC; uc001vcu.4; human. [Q9BWV3-1]
DR CTD; 81602; -.
DR DisGeNET; 81602; -.
DR GeneCards; CDADC1; -.
DR HGNC; HGNC:20299; CDADC1.
DR HPA; ENSG00000102543; Low tissue specificity.
DR MIM; 618997; gene.
DR neXtProt; NX_Q9BWV3; -.
DR OpenTargets; ENSG00000102543; -.
DR PharmGKB; PA134884656; -.
DR VEuPathDB; HostDB:ENSG00000102543; -.
DR eggNOG; KOG3127; Eukaryota.
DR GeneTree; ENSGT00940000153676; -.
DR HOGENOM; CLU_038832_1_0_1; -.
DR InParanoid; Q9BWV3; -.
DR OMA; ACRQERI; -.
DR OrthoDB; 1569973at2759; -.
DR PhylomeDB; Q9BWV3; -.
DR TreeFam; TF333295; -.
DR PathwayCommons; Q9BWV3; -.
DR SignaLink; Q9BWV3; -.
DR BioGRID-ORCS; 81602; 17 hits in 1081 CRISPR screens.
DR ChiTaRS; CDADC1; human.
DR GenomeRNAi; 81602; -.
DR Pharos; Q9BWV3; Tbio.
DR PRO; PR:Q9BWV3; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9BWV3; protein.
DR Bgee; ENSG00000102543; Expressed in sperm and 175 other tissues.
DR ExpressionAtlas; Q9BWV3; baseline and differential.
DR Genevisible; Q9BWV3; HS.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0004126; F:cytidine deaminase activity; IDA:UniProtKB.
DR GO; GO:0061676; F:importin-alpha family protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IMP:UniProtKB.
DR GO; GO:0009972; P:cytidine deamination; IDA:UniProtKB.
DR GO; GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB.
DR CDD; cd01286; deoxycytidylate_deaminase; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR015517; dCMP_deaminase-rel.
DR InterPro; IPR035105; Deoxycytidylate_deaminase_dom.
DR PANTHER; PTHR11086; PTHR11086; 1.
DR Pfam; PF00383; dCMP_cyt_deam_1; 2.
DR SUPFAM; SSF53927; SSF53927; 2.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..514
FT /note="Cytidine and dCMP deaminase domain-containing
FT protein 1"
FT /id="PRO_0000300491"
FT DOMAIN 70..168
FT /note="CMP/dCMP-type deaminase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT DOMAIN 317..482
FT /note="CMP/dCMP-type deaminase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 271..283
FT /note="Nuclear export signal"
FT /evidence="ECO:0000305|PubMed:26945630"
FT MOTIF 488..510
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:26945630"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT VAR_SEQ 1..380
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027811"
FT VAR_SEQ 85..99
FT /note="VKRTGLVVVKNMKIV -> KTMFCLFENDCKCWS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027812"
FT VAR_SEQ 100..514
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027813"
FT VAR_SEQ 144..154
FT /note="AGVNRISYWPA -> GLLGAAKMPR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027814"
FT VAR_SEQ 155..514
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027815"
SQ SEQUENCE 514 AA; 58455 MW; 6560103A65C03D69 CRC64;
MKEAGQMQNL ESARAGRSVS TQTGSMTGQI PRLSKVNLFT LLSLWMELFP AEAQRQKSQK
NEEGKHGPLG DNEERTRVST DKRQVKRTGL VVVKNMKIVG LHCSSEDLHA GQIALIKHGS
RLKNCDLYFS RKPCSACLKM IVNAGVNRIS YWPADPEISL LTEASSSEDA KLDAKAVERL
KSNSRAHVCV LLQPLVCYMV QFVEETSYKC DFIQKITKTL PDANTDFYYE CKQERIKEYE
MLFLVSNEEM HKQILMTIGL ENLCENPYFS NLRQNMKDLI LLLATVASSV PNFKHFGFYR
SNPEQINEIH NQSLPQEIAR HCMVQARLLA YRTEDHKTGV GAVIWAEGKS RSCDGTGAMY
FVGCGYNAFP VGSEYADFPH MDDKQKDREI RKFRYIIHAE QNALTFRCQE IKPEERSMIF
VTKCPCDECV PLIKGAGIKQ IYAGDVDVGK KKADISYMRF GELEGVSKFT WQLNPSGAYG
LEQNEPERRE NGVLRPVPQK EEQHQDKKLR LGIH
